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Database: UniProt
Entry: A0A0D2IB95_9EURO
LinkDB: A0A0D2IB95_9EURO
Original site: A0A0D2IB95_9EURO 
ID   A0A0D2IB95_9EURO        Unreviewed;       523 AA.
AC   A0A0D2IB95;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN   ORFNames=Z518_06649 {ECO:0000313|EMBL:KIX03099.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX03099.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX03099.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX03099.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a
CC       regulatory module of the Mediator complex which is itself involved in
CC       regulation of basal and activated RNA polymerase II-dependent
CC       transcription. The SRB8-11 complex may be involved in the
CC       transcriptional repression of a subset of genes regulated by Mediator.
CC       It may inhibit the association of the Mediator complex with RNA
CC       polymerase II to form the holoenzyme complex. The SRB8-11 complex
CC       phosphorylates the C-terminal domain (CTD) of the largest subunit of
CC       RNA polymerase II. {ECO:0000256|ARBA:ARBA00025278}.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   EMBL; KN847479; KIX03099.1; -; Genomic_DNA.
DR   RefSeq; XP_013270235.1; XM_013414781.1.
DR   AlphaFoldDB; A0A0D2IB95; -.
DR   STRING; 1442369.A0A0D2IB95; -.
DR   GeneID; 25294720; -.
DR   VEuPathDB; FungiDB:Z518_06649; -.
DR   HOGENOM; CLU_022000_7_2_1; -.
DR   OrthoDB; 4848277at2759; -.
DR   Proteomes; UP000053617; Unassembled WGS sequence.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd20545; CYCLIN_SpCG1C-like_rpt1; 1.
DR   CDD; cd20546; CYCLIN_SpCG1C_ScCTK2-like_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR043198; Cyclin/Ssn8.
DR   InterPro; IPR006671; Cyclin_N.
DR   PANTHER; PTHR10026; CYCLIN; 1.
DR   PANTHER; PTHR10026:SF51; CYCLIN-T; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF036580; Cyclin_L; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Cyclin {ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053617}.
FT   DOMAIN          60..168
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          274..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  59447 MW;  A7E3F047D6A5DB4B CRC64;
     MPAFRKTPQP GALPLFSTNP VLERTQSQWL FTAEELCRSP SILNGMPVAQ ELANRQKGVN
     FITQVGIMLK LPQLTLATAS VYLHRFFMRH EMVQPGQKGQ QGFHHYSVAA TAIFLATKVE
     ENYRKMRELV VACCRVAQKQ PNLVVDEQSK EYWKWRDNIL HNEDLLLEAL CFDLQLEQPY
     RILLDYLRFY RVQENKLLRN TSWAFLNDSL VTTMCLQLTP SAIAGSALYI GVKFAGITLP
     DDERGRPWWE QLGLGLHDLQ RGCNLMAEVY ENPTLPRQGQ KEAYTRDDDF SMFDRTRQAT
     SPQPDRSPAL STRSGSQGAK RDRDTADDPN SGEWGSSLTA RPPGENLWQP SPKRARRDSR
     DDTSNLPERA MQRIPSRGVD DPSDHDSREH VDDVQKRIDD IVNNSASSRV PRPGLPRRAS
     HQPSYQSHSS RRHSSSGSNW NGPPSSSSNG HQDRVLPQSR PVSRDSDHYH QNDQYDPQRM
     ASRIPPPSVN ERPFPPQPEQ FPNGINDLDD AEKVDYGSEE GEL
//
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